换一批Biochemical and structural studies of the oligomerization domain of the Nipah virus phosphoprotein: evidence for an elongated coiled-coil homotrimer.
第一作者：
David,Blocquel
第一单位：
CNRS and Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), UMR 7257, 13288 Marseille, France.
作者：
关键词
2,2,2-trifluoroethanolAnalytical ultracentrifugationCDCoiled-coilCross-linkingGFHeVHendra virusHenipavirusHomotrimerIMACLMALDI-TOFMREMeVMuVNNMRNiVNipah virusODPP C-terminal domainP N-terminal domainP multimerization domainPCRPCTPMDPNTPhosphoproteinR(S)R(g)RDVRSVRVRinderpest virusSABSAXSSDS-PAGESeVSendai virusSmall-angle X-ray scatteringStokes radiusSuberic acid bis (N-hydroxy-succinimide ester)T(m)TFEVSVX domain of PXDcircular dichroismgel filtrationimmobilized metal affinity chromatographylarge proteinmatrix-assisted laser desorption ionization/time of flightmean ellipticity values per residuemeasles virusmelting temperaturemumps virusnuclear magnetic resonancenucleoproteinoptical densityphosphoproteinpolymerase chain reactionrabies virusradius of gyrationrespiratory syncytial virussmall angle X-ray scatteringsodium dodecyl sulphate polyacrylamide electrophoresisvesicular stomatitis virus
医学主题词
人类(Humans);尼帕病毒(Nipah Virus);磷蛋白类(Phosphoproteins);蛋白质构象(Protein Conformation);蛋白质相互作用域和基序(Protein Interaction Domains and Motifs);蛋白质多聚化(Protein Multimerization);散射, 小角(Scattering, Small Angle);超速离心法(Ultracentrifugation);病毒蛋白质类(Viral Proteins)
DOI
10.1016/j.virol.2013.07.031
PMID
24074578
发布时间
2013-09-30
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Virology
162-72页
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